Segmental isotopic labeling of HIV-1 capsid protein assemblies for solid state NMR

Journal of Biomolecular NMR
Sebanti Gupta, Robert Tycko

Abstract

Recent studies of noncrystalline HIV-1 capsid protein (CA) assemblies by our laboratory and by Polenova and coworkers (Protein Sci 19:716-730, 2010; J Mol Biol 426:1109-1127, 2014; J Biol Chem 291:13098-13112, 2016; J Am Chem Soc 138:8538-8546, 2016; J Am Chem Soc 138:12029-12032, 2016; J Am Chem Soc 134:6455-6466, 2012; J Am Chem Soc 132:1976-1987, 2010; J Am Chem Soc 135:17793-17803, 2013; Proc Natl Acad Sci USA 112:14617-14622, 2015; J Am Chem Soc 138:14066-14075, 2016) have established the capability of solid state nuclear magnetic resonance (NMR) measurements to provide site-specific structural and dynamical information that is not available from other types of measurements. Nonetheless, the relatively high molecular weight of HIV-1 CA leads to congestion of solid state NMR spectra of fully isotopically labeled assemblies that has been an impediment to further progress. Here we describe an efficient protocol for production of segmentally labeled HIV-1 CA samples in which either the N-terminal domain (NTD) or the C-terminal domain (CTD) is uniformly 15N,13C-labeled. Segmental labeling is achieved by trans-splicing, using the DnaE split intein. Comparisons of two-dimensional solid state NMR spectra of fully labeled and segme...Continue Reading

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Citations

Feb 9, 2019·Current Protein & Peptide Science·Corina Sarmiento, Julio A Camarero
Apr 29, 2020·Proceedings of the National Academy of Sciences of the United States of America·Sebanti GuptaRobert Tycko
May 31, 2020·Progress in Nuclear Magnetic Resonance Spectroscopy·Thomas Wiegand
Sep 30, 2020·Viruses·Lauriane LecoqAnja Böckmann
Apr 30, 2021·Current Opinion in Structural Biology·Marta BonaccorsiGuido Pintacuda
Dec 12, 2018·Progress in Nuclear Magnetic Resonance Spectroscopy·Jean-Philippe DemersAdam Lange
Sep 30, 2021·Annual Review of Virology·Gal Porat-DahlerbruchTatyana Polenova

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